| Effects of human collagen メ-1 type I-derived proteins on collagen synthesis and elastin production in human dermal fibroblasts |
Su Jin Hwang1,# (Researcher), Su Hwan Kim2,# (Graduate student), Woo-Young Seo1 (Research worker), Yelin Jeong3,4 (Graduate student), Min Cheol Shin3,4 (Graduate student), Dongryeol Ryu5 (Professor), Sang Bae Lee6 (Professor), Young Jin Choi2,7,8 (Professor), KyeongJin Kim  3,4,* (Professor) |
1ABIOTECH Co., Ltd,
2Department of Agricultural Biotechnology, Seoul National University,
3Department of Biomedical Sciences, Inha University College of Medicine,
4Program in Biomedical Science & Engineering, Inha University,
5Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine,
6Division of Life Sciences, Jeonbuk National University,
7Center for Food and Bioconvergence and 8Research Institute for Agriculture and Life Sciences, Seoul National University |
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Abstract
Collagen type I is the most abundant form of collagen in human tissues, and is composed of two identical メ-1 type I chains and an メ-2 type I chain organized in a triple helical structure. A previous study has shown that human collagen メ-2 type I (hCOL1A2) promotes collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). However, the biological effects of human collagen メ-1 type I (hCOL1A1) on various skin properties have not been investigated. Here, we isolate and identify the hCOL1A1-collagen effective domain (CED) which promotes collagen type I synthesis. Recombinant hCOL1A1-CED effectively induces cell proliferation and collagen biosynthesis in HDFs, as well as increased cell migration and elastin production. Based on these results, hCOL1A1-CED may be explored further for its potential use as a preventative agent against skin aging.
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| Abstract, Accepted Manuscript(in press) [Submitted on March 9, 2021, Accepted on April 26, 2021] |
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